Cheminformatics and Computational Chemical Biology

Biography

Biography: Nuzhat Gull

Abstract

In the present study the cationic gemini surfactant assisted refolding of guanidinium hydrochloride (GndHcl) denatured mammalian serum albumins viz. sheep serum albumin (SSA), rat serum albumin (RSA) and porcine serum albumin (PSA) using a combination of cationic gemini surfactants, pentanediyl-a,w-bis(cety|dimethylammonium bromide (C16H33(CH3)2N+—(CH2)5—N+(CH3)2C16H33).2Br-designated as GS and methyl- [3-cyclodextrin in the artificial chaperone assisted two step method, is attempted The studies were carried out in an aqueous medium (pH 7‘4) using dynamic light scattering (DLS), circular dichroism (CD), and fluorescence spectroscopy‘ A perusal of DLS data indicates that against the native hydrodynamic radius (Rh) of 43 nm in SSA, 3.9 nm in PSA and 35 nm in RSA, the Rh of the said proteins, when refolding is attempted by simple dilution, increases to 217nm, 36.6 nm and 372 nm, respectively‘ Hydrodynamic radii very near to the native protein, Le, 40 nm, 41 nm and 4.4 nm for RSA, PSA and SSA respectively, is obtained on the sequential addition of GS and methyl-B-cyclodextrin to the denatured protein. Circular dichroism studies corroborate with the DLS data. The results obtained from the multi-technique approach are ascribed to the presence of two charged head-groups and two hydrocarbon tails in the gemini surfactants resulting in very strong electrostatic and hydrophobic interactions Based on the present study it is suggested that gemini surfactants may be utilized in the protein refolding studies and thus may address one of the most pressing demand of biotechnology industry for the development of efficient and inexpensive folding aides.